ID A0A0G8AR50_9SYNE Unreviewed; 655 AA.
AC A0A0G8AR50;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Ribonuclease J {ECO:0000313|EMBL:KKZ09969.1};
DE Flags: Fragment;
GN ORFNames=TQ37_10440 {ECO:0000313|EMBL:KKZ09969.1};
OS Candidatus Synechococcus spongiarum 15L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1608419 {ECO:0000313|EMBL:KKZ09969.1, ECO:0000313|Proteomes:UP000035037};
RN [1] {ECO:0000313|EMBL:KKZ09969.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ09969.1};
RA Slaby B., Hentschel U.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKZ09969.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ09969.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKZ09969.1}.
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DR EMBL; JYFQ01000224; KKZ09969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G8AR50; -.
DR STRING; 431041.FLM9_794; -.
DR PATRIC; fig|1608419.3.peg.1429; -.
DR Proteomes; UP000035037; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd07714; RNaseJ_MBL-fold; 1.
DR Gene3D; 3.10.20.580; -; 1.
DR Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR InterPro; IPR001587; RNase_J_CS.
DR NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS01292; UPF0036; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..203
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 552..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKZ09969.1"
SQ SEQUENCE 655 AA; 71862 MW; D793C4AA36377D27 CRC64;
GLHEIGKNTC VFEYGNELML VDAGLSFPSD DMHGVNVVVP DTTYLRENQQ RIRGMIVTHG
HEDHIGGIAH HLKQFTIPVI YGPRLALSLL DDKMKEAGVS DRTGTRTVRP REVVKVGKNF
SVEFIRNTHS IADSFSLAIT TPVGVVVFTG DFKFDHTPVD GERFDLHRLA RYGEDGVLCL
FSDSTNAELP GFTPPERSVF PNLDRHVAQA KGRVLVTTFA SSVHRVSMIL ELALKHGRRV
GLLGRSMLNV IAKARELGYI RCPDDLFLTM KQLRDLPERE LLLLMTGSQG EHLAALSRIA
RAEHPHVQLK STDTVIFSAS PIPGNTIGVV KVIDQLMMQG ATVIYGKDKG IHVSGHGSQE
DEKLMLALTR PKFFVPVHGE HRMLVQHCKT AQSMGIPAES MLVIENGDVV ELTPESIRRG
EPVKAGIELL DSSRKGVINT QVLKERQQLA EDGVLVAHVS VSSAGHMGAP ARVNLRGVAT
SLAPQHFANW TDNEVQWVLD NRWQQLCRGG DDLQDVDWVG LQREVELGLQ RRLRRELEVA
PLIIVVVQPT PKGSTAVYKP DTEEKGAPGH MGRGGGRHQG ARPLQRNGSS NGQSRNPALM
DRRPLSTHGS NSTMAPPSTV PSSVASSEPE VKANGVEPGV ETERKRRSRS RTSPA
//
